ID A0A367FQE3_9ACTN Unreviewed; 1044 AA.
AC A0A367FQE3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:RCG32062.1};
GN ORFNames=DQ384_05920 {ECO:0000313|EMBL:RCG32062.1};
OS Sphaerisporangium album.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sphaerisporangium.
OX NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG32062.1, ECO:0000313|Proteomes:UP000253094};
RN [1] {ECO:0000313|EMBL:RCG32062.1, ECO:0000313|Proteomes:UP000253094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG32062.1,
RC ECO:0000313|Proteomes:UP000253094};
RA Li L.;
RT "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT the South China Sea.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCG32062.1}.
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DR EMBL; QOIL01000003; RCG32062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367FQE3; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000253094; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034213; S8_Vpr-like.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000253094};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1044
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017084487"
FT DOMAIN 95..146
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 174..627
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 435..519
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 1025..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 252
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 590
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1044 AA; 105169 MW; 0C0BEEEE99D646AC CRC64;
MKRRLLFGAV LASASVAIPP AVIPSTANAE PARPPAFQHL PGTYNYSGFR PAVLDTARSL
KVLIQVTGTP VGDAAADAED AGRSVDKPSL RSALRTERQS VEEKVKAEGG KVLATYTDSF
NGIAATIPAR SLSAIAETPK VVSVHPVRTF SRDNTAGVPY IGAPQVWQDL GKTGDGVKVA
IIDTGVDYTH ANFGGSGDPA DFERNDGTVI EPGTFPTAKV IGGYDFVGDD YDDNIPTSVP
KPDPDPLDCN GHGSHVAGSA AGFGVDAGGR TYAGPYDSTT HSKSFKIGPG VAPKALIMAY
RVFGCEGSAS EDVIVSAMER ALKDGANVVN MSLGSPFGRV DEPSAQAVRT LTRAGVTVVA
SAGNSGPNAY ITGAPAVAPT AISVAALDAA RAQLPAAKIS ADGTEIVAQN SNEAALPSGT
LPIAVLRTSY PSGPVSLGCD PADYTAYPGG VTGKLVITLR GVCARVKRAI LGQKAGAAAV
AMINTDAAYP PIEGPITSDP DTGEPYTVTI PFLGIKSTDR AAATSLDGKS TALTAMAVPN
PGYAKLASFS SGGPGNGASA LKPDVTAPGV AIVSTGVGTG SGPATISGTS MASPMTAGVA
ALVKQAHPRW RPGQIKAAIV STADASTKIA GYTARVAGSG VVAARQAVAA TVLGETGHGG
GNLSFGLQSL TGAYRQSETF TIRNTGKASV TYDLAAAFTG QSYGAQATVS PASVTVGPES
SRDVRVTLSL TAQAVAALPA AETSNFGSLV HIQGAVTATP RAAAEGVYPL RAAFLLVPDA
QSEATTSQPG KYTVSGGVAA TSVKVQNKGA HAGAADVYAW GITDSEDVRG AEDSMDVRAA
GVQALPGSVL GGADTDRTLV FAVNTSGRWS NASANEFDIP IDVTGDGTAD YVLVGADYGL
VTAGSSDGRF ATFVFKADGS LVDTWVATAP MNGGTLLMPV LASQVGLAEG ASRFTYSVSA
SSKVPAGLVD DTEPAAFDAF APAVSTGAYV PLEPGASSTI ALTADPARLA STPVKGWLVV
SLDDRSGSPE ADKVPLGKVP TVKP
//
